B0SRF1

PR
Gene name
dnaK
Protein name
Chaperone protein DnaK
Names
HSP70, Heat shock 70 kDa protein, Heat shock protein 70
Species
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
KEGG Pathway
lbi:LEPBI_I3379
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

575-644 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B0SRF1

Entry ID Method Resolution Chain Position Source
AF-B0SRF1-F1 Predicted AlphaFoldDB

No variants for B0SRF1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0SRF1

No associated diseases with B0SRF1

2 regional properties for B0SRF1

Type Name Position InterPro Accession
conserved_site Heat shock protein 70, conserved site 9 - 16 IPR018181-1
conserved_site Heat shock protein 70, conserved site 192 - 205 IPR018181-2

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
unfolded protein binding Binding to an unfolded protein.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSKEKIIGID LGTTNSCVAV MEGGDPVVIQ NSEGARTTPS IVAFTAKGET IVGQFAKNQA
70 80 90 100 110 120
ITNAVNTIRS AKRFIGRRFN EAGDESKMVS YKVIRAGNDG VKFETVSGEF TPQEIAARVL
130 140 150 160 170 180
QKMKKTAEDF LGHEVKKAVV TVPAYFNDEQ RQATKDAGRI AGLEVERIIN EPTAAALAYG
190 200 210 220 230 240
FDKKKTNAKI AVYDLGGGTF DVSILELGDG VFEVKSTNGD THLGGDDFDN VVMQWMIDEF
250 260 270 280 290 300
KKQTGIDISG DKNTVQRLKE AAEKAKIELS GTSSTQINLP FITADASGPK HLDMTLTKAK
310 320 330 340 350 360
FDEITRSLVE RTRIPCINAL KDAGLSASEI DEVILVGGSI RIPAVQALVK EIFGKEPNKS
370 380 390 400 410 420
VNPDEVVAVG AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVMTKLIER NTTIPTRKSQ
430 440 450 460 470 480
VFSTAADNQT TVSVHVLQGE REMASANRTL GRFDLVGIPS APRGVPQIEV TFDIDANGIV
490 500 510 520 530 540
HVSAKDLGTG KEQKIRIESS SGLSEEEIKK MVKDAEAHAE EDKKLREAAD TKNELEAIVY
550 560 570 580 590 600
QLEKTIGESA DKLDESEKQR AQDEIKRGRE AMESGDLERM KASRDSIQQV AMQIGQKIYS
610 620 630 640
QAGPEQGAPG AEAGAGASQG ASGTDANGEK VVDADYTVVD EDKK